Crystallization of the calcium-activated phosphoenolpyruvate carboxykinase from Escherichia coli K12

Delbaere, L. T. J.; Vandonselaar, M.; Glaeske, D; Jabs, Corrine; Goldie, Hughes

doi:10.1016/0022-2836(91)90654-o

Journal of Molecular Biology

1991

DOI: 10.1016/0022-2836(91)90654-o

|View full text |Cite

Crystallization of the calcium-activated phosphoenolpyruvate carboxykinase from Escherichia coli K12

L. T. J. Delbaere

M. Vandonselaar

D Glaeske

et al.

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...

Citation Types

Supporting

Mentioning

Contrasting

Year Published

1993

2021

Publication Types

Select...

Article6

Relationship

Self Cite1

Independent5

Authors

Journals

Cited by 8 publications

(1 citation statement)

References 14 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Crystal Structure of E. coli PCK Tertiary Structure-X-ray quality crystals of E. coli PCK were originally obtained in 1991 (27) and led to the structure determination using multiple isomorphous replacement and electron density modification techniques, followed by refinement against 1.9-Å resolution synchrotron data (23). The structure of the ATP-Mg 2ϩ -oxalate ternary complex of E. coli PCK was subsequently solved at 1.8-Å resolution by molecular replacement techniques (25).…”

mentioning

confidence: 99%

Structure and Mechanism of Phosphoenolpyruvate Carboxykinase

Matte¹,

Tari²,

Goldie

et al. 1997

Journal of Biological Chemistry

Self Cite

136

108

View full text Add to dashboard Cite

mentioning

confidence: 99%

Structure and Mechanism of Phosphoenolpyruvate Carboxykinase

Matte¹,

Tari²,

Goldie

et al. 1997

Journal of Biological Chemistry

Self Cite

136

108

View full text Add to dashboard Cite

Reactivity of cysteinyl, arginyl, and lysyl residues ofEscherichia coli phosphoenolpyruvate carboxykinase against group-specific chemical reagents

et al. 1993

View full text Add to dashboard Cite

Calcium-activated phosphoenolpyruvate carboxykinase from Escherichia coli is not inactivated by a number of sulfhydryl-directed reagents [5,5'-dithiobis(2-nitrobenzoate), iodoacetate, N-ethylmaleimide, N-(1-pyrenyl)maleimide or N-(iodoacetyl)-N'-(5-sulfo-1-naphthylethylenediamine)], unlike phosphoenolpyruvate carboxykinase from other organisms. On the other hand, the enzyme is rapidly inactivated by the arginyl-directed reagents 2,3-butanedione and 1-pyrenylglyoxal. The substrates, ADP plus PEP in the presence of Mn2+, protect the enzyme against inactivation by the diones. Quantitation of pyrenylglyoxal incorporation indicates that complete inactivation correlates with the binding of one inactivator molecule per mole of enzyme. Chemical modification by pyridoxal 5'-phosphate also produces inactivation of the enzyme, and the labeled protein shows a difference spectrum with a peak at 325 nm, characteristic of a pyridoxyl derivative of lysine. The inactivation by this reagent is also prevented by the substrates. Binding stoichiometries of 1.25 and 0.30 mol of reagent incorporated per mole of enzyme were found in the absence and presence of substrates, respectively. The results suggest the presence of functional arginyl and lysyl residues in or near the active site of the enzyme, and indicate lack of reactive functional sulfhydryl groups.

show abstract

Comparative steady-state fluorescence studies of cytosolic rat liver (GTP), Saccharomyces cerevisiae (ATP) and Escherichia coli (ATP) phosphoenolpyruvate carboxykinases

Encinas

Rojas

Goldie

et al. 1993

Biochimica et Biophysica Acta (BBA) - Protein Structure and Mol

View full text Add to dashboard Cite

scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.

Contact Info

customersupport@researchsolutions.com

10624 S. Eastern Ave., Ste. A-614

Henderson, NV 89052, USA

This site is protected by reCAPTCHA and the Google Privacy Policy and Terms of Service apply.

Blog Terms and Conditions API Terms Privacy Policy Contact Cookie Preferences Do Not Sell or Share My Personal Information

Made with 💙 for researchers

Part of the Research Solutions Family.

Crystallization of the calcium-activated phosphoenolpyruvate carboxykinase from Escherichia coli K12

Cited by 8 publications

References 14 publications

Structure and Mechanism of Phosphoenolpyruvate Carboxykinase

Structure and Mechanism of Phosphoenolpyruvate Carboxykinase

Reactivity of cysteinyl, arginyl, and lysyl residues ofEscherichia coli phosphoenolpyruvate carboxykinase against group-specific chemical reagents

Comparative steady-state fluorescence studies of cytosolic rat liver (GTP), Saccharomyces cerevisiae (ATP) and Escherichia coli (ATP) phosphoenolpyruvate carboxykinases

Contact Info

Product

Resources

About